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Originally published In Press as doi:10.1074/jbc.M100506200 on July 6, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33645-33651, September 7, 2001
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Identification and Characterization of SppA, a Novel Light-inducible Chloroplast Protease Complex Associated with Thylakoid Membranes*

Martin Lensch, Reinhold G. Herrmann, and Anna SokolenkoDagger

From the Botanisches Institut der Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-80638 München, Germany

A new component of the chloroplast proteolytic machinery from Arabidopsis thaliana was identified as a SppA-type protease. The sequence of the mature protein, deduced from a full-length cDNA, displays 22% identity to the serine-type protease IV (SppA) from Escherichia coli and 27% identity to Synechocystis SppA1 (sll1703) but lacks the putative transmembrane spanning segments predicted from the E. coli sequence. The N-terminal sequence exhibits typical features of a cleavable chloroplast stroma-targeting sequence. The chloroplast localization of SppA was confirmed by in organello import experiments using an in vitro expression system and by immunodetection with antigen-specific antisera. Subfractionation of intact chloroplasts demonstrated that SppA is associated exclusively with thylakoid membranes, predominantly stroma lamellae, and is a part of some high molecular mass complex of about 270 kDa that exhibits proteolytic activity. Treatments with chaotropic salts and proteases showed that SppA is largely exposed to the stroma but that it behaves as an intrinsic membrane protein that may have an unusual monotopic arrangement in the thylakoids. We demonstrate that SppA is a light-inducible protease and discuss its possible involvement in the light-dependent degradation of antenna and photosystem II complexes that both involve serine-type proteases.


* This work was supported by Deutsche Forschungsgemeinschaft Grant DFG SO448/2-1 (to A. S.) and SFB 184 (to R. H.) and the Fonds der Chemischen Industrie.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 49-89-17861242; Fax: 49-89-1782274; E-mail: anna@botanik.biologie.uni-muenchen.d.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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